Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127   2 QEEKSKEDHSRLINVTAKDLTVRNrrLVEVPYTATLSHAMNTLVANSISALPVaappghwigaggsmimesdkqtgVVRK 81
Cdd:COG2524  72 VRVVAEKELGLVLKMKVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPV-----------------------VDDG 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127  82 HYIGILTMLDILAHIAgedsnlsDLDRKMSSQVSSIIGHcleglSLWTLNPNTSVLECMEVFSK-GIHRALVpvessIES 160
Cdd:COG2524 127 KLVGIITERDLLKALA-------EGRDLLDAPVSDIMTR-----DVVTVSEDDSLEEALRLMLEhGIGRLPV-----VDD 189

                       170       180
                ....*....|....*....|....*...
gi 15218127 161 NNTIAGVeliesasaykmLTQMDLLRFL 188
Cdd:COG2524 190 DGKLVGI-----------ITRTDILRAL 206

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15218127    300 EVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSL 347
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15218127 301 VVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSL 347
Cdd:cd04641  77 VHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYL 123

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127  25 NRRLVEVPYTATLSHAMNTLVANSISALPVAAPPGHwigaggsmimesdkqtgvvrkhYIGILTMLDILAHIAGEDSNLS 104
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK----------------------LVGIVTERDILRALVEGGLALD 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 105 DLDRK-MSSQVSsiighcleglslwTLNPNTSVLECMEVFSK-GIHRalVPVessIESNNTIAGveliesasaykMLTQM 182
Cdd:cd02205  59 TPVAEvMTPDVI-------------TVSPDTDLEEALELMLEhGIRR--LPV---VDDDGKLVG-----------IVTRR 109

                ....
gi 15218127 183 DLLR 186
Cdd:cd02205 110 DILR 113

CBS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 211 NDSVYAITERTTVSNAINVMKGALLNAVPIVHApdiaqedhlqlvngrHRKVIGTFSATDLKGCRLPELQTWLPLTALEF 290
Cdd:COG0517   8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDE---------------DGKLVGIVTDRDLRRALAAEGKDLLDTPVSEV 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218127 291 -TektsgkeREVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSLR 348
Cdd:COG0517  73 mT-------RPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15218127   299 REVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSLRS 349
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 211 NDSVYAITERTTVSNAINVMKGALLNAVPIVHapdiaqedhlqlvngRHRKVIGTFSATDLKGcRLPELQTWLPLTALEF 290
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVD---------------DDGKLVGIVTERDILR-ALVEGGLALDTPVAEV 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15218127 291 TEktsgkeREVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIR 345
Cdd:cd02205  65 MT------PDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 214 VYAITERTTVSNAINVMKGALLNAVPIVhapdiaqedhlqlvnGRHRKVIGTFSATDL----KGCRLPELQTWLPLTALE 289
Cdd:cd04586   5 VVTVTPDTSVREAARLLLEHRISGLPVV---------------DDDGKLVGIVSEGDLlrreEPGTEPRRVWWLDALLES 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218127 290 FTE------KTSGKE------REVVSCGVESTMEEAIEKVVTRGVHRVWVMDqQGLLQGVVSLTDIIR 345
Cdd:cd04586  70 PERlaeeyvKAHGRTvgdvmtRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLLR 136

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127   2 QEEKSKEDHSRLINVTAKDLTVRNrrLVEVPYTATLSHAMNTLVANSISALPVaappghwigaggsmimesdkqtgVVRK 81
Cdd:COG2524  72 VRVVAEKELGLVLKMKVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPV-----------------------VDDG 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127  82 HYIGILTMLDILAHIAgedsnlsDLDRKMSSQVSSIIGHcleglSLWTLNPNTSVLECMEVFSK-GIHRALVpvessIES 160
Cdd:COG2524 127 KLVGIITERDLLKALA-------EGRDLLDAPVSDIMTR-----DVVTVSEDDSLEEALRLMLEhGIGRLPV-----VDD 189

                       170       180
                ....*....|....*....|....*...
gi 15218127 161 NNTIAGVeliesasaykmLTQMDLLRFL 188
Cdd:COG2524 190 DGKLVGI-----------ITRTDILRAL 206

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 211 NDSVYAITERTTVSNAINVMKGALLNAVPIVHAPDiaqedhlqlvngrhrKVIGTFSATDLKGCRLPELQTWLPLTALEF 290
Cdd:COG2905   6 SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDG---------------RLVGIITDRDLRRRVLAEGLDPLDTPVSEV 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218127 291 TEktsgkeREVVSCGVESTMEEAIEKVVTRGVHRVWVMDqQGLLQGVVSLTDIIRSLRS 349
Cdd:COG2905  71 MT------RPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSE 122

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127  25 NRRLVEVPYTATLSHAMNTLVANSISALPVAAPPGHwigaggsmimesdkqtgvvrkhYIGILTMLDILAHIAGEDSNLS 104
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK----------------------LVGIVTERDILRALVEGGLALD 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 105 DLDRK-MSSQVSsiighcleglslwTLNPNTSVLECMEVFSK-GIHRalVPVessIESNNTIAGveliesasaykMLTQM 182
Cdd:cd02205  59 TPVAEvMTPDVI-------------TVSPDTDLEEALELMLEhGIRR--LPV---VDDDGKLVG-----------IVTRR 109

                ....
gi 15218127 183 DLLR 186
Cdd:cd02205 110 DILR 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218127 299 REVVSCGVESTMEEAIEKVVTRG-----VHRVWVMDQQGLLQGVVSLTDIIRSLRSTL 351
Cdd:cd04606   9 TEFVAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLADPDTK 66

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15218127 299 REVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDI 343
Cdd:cd04622  68 GDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15218127 299 REVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSL 347
Cdd:cd17775  69 ADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

CBS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 129 TLNPNTSVLECMEVFSKGiHRALVPVessIESNNTIAGveliesasaykMLTQMDLLRFLKDHHFDdlktVLSRSISDLg 208
Cdd:COG0517  13 TVSPDATVREALELMSEK-RIGGLPV---VDEDGKLVG-----------IVTDRDLRRALAAEGKD----LLDTPVSEV- 72

                        90       100       110
                ....*....|....*....|....*....|...
gi 15218127 209 aVNDSVYAITERTTVSNAINVMKGALLNAVPIV 241
Cdd:COG0517  73 -MTRPPVTVSPDTSLEEAAELMEEHKIRRLPVV 104

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15218127 299 REVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRSL 347
Cdd:cd09836  67 KNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218127 299 REVVSCGVESTMEEAIEKVVTRG-----VHRVWVMDQQGLLQGVVSLTDIIRSLRSTL 351
Cdd:COG2239 137 TEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLLLADPDTK 194

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 129 TLNPNTSVLECMEVFSK-GIHRALVpvessIESNNTIAGveliesasaykMLTQMDLLRFLKDHHFDDLKTVlsrsiSDL 207
Cdd:cd02205   6 TVDPDTTVREALELMAEnGIGALPV-----VDDDGKLVG-----------IVTERDILRALVEGGLALDTPV-----AEV 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218127 208 gaVNDSVYAITERTTVSNAINVMKGALLNAVPIVhapdiaqedhlqlvnGRHRKVIGTFSATDL 271
Cdd:cd02205  65 --MTPDVITVSPDTDLEEALELMLEHGIRRLPVV---------------DDDGKLVGIVTRRDI 111

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218127 214 VYAITERTTVSNAINVMKGALLNAVPIVHapdiaqedhlqlvNGrhrKVIGTFSATDLKGCrlpelqtwlpltalEFTEK 293
Cdd:cd04610   5 VITVSPDDTVKDVIKLIKETGHDGFPVVD-------------DG---KVVGYVTAKDLLGK--------------DDDEK 54

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15218127 294 TSGK-EREVVSCGVESTMEEAIEKVVTRGVHRVWVMDQQGLLQGVVSLTDIIRS 346
Cdd:cd04610  55 VSEImSRDTVVADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVIRS 108